Ganesh, C and Banerjee, Antara and Shah, Aseema and Varadarajan, Raghavan (1999) Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein. In: FEBS Letters, 454 (3). pp. 307-311.
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Maltose binding protein (MBP) exhibits a slow phase of folding at pH 7.4, 298 K. The kinetics of this phase has been characterized as a function of denaturant concentration and temperature. Denaturant double-jump experiments and the activation energy for folding indicate that the slow phase involves processes other than proline isomerization. Although the first five N-terminal residues are disordered in the MBP crystal structure, mutations in this region slow down folding and destabilize the native structure. This is the first report showing that disordered N-terminal residues can affect folding kinetics and stability.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Federation of European Biochemical Societies.|
|Keywords:||Folding;Kinetics;Stability;Maltose binding protein;Double jump;Mass spectrometry|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||16 Oct 2007|
|Last Modified:||19 Sep 2010 04:40|
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